Differences in the functional interaction of two purified cytochrome P-450 isozymes with epoxide hydrolase.
The relative functional associations of two cytochrome P-450 isozymes with epoxide hydrolase were investigated in a reconstituted system containing highly purified enzymes. Cytochromes P-450 PB-B, the major hepatic form from phenobarbital-induced rats, and BNF-B, the major form from beta-naphthoflavone-induced rats, were compared, with naphthalene and 2,3- and 2,5-dichlorobiphenyl as substrates. The results indicate that cytochrome P-450 BNF-B is more firmly associated with epoxide hydrolase than is cytochrome P-450 PB-B, and the association has major consequences for chemical carcinogenicity and toxicology.
D000818:Animals; D001571:Benzoflavones / Q000494:pharmacology; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004851:Epoxide Hydrolases / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D009281:Naphthalenes / Q000378:metabolism; D010634:Phenobarbital / Q000494:pharmacology; D011078:Polychlorinated Biphenyls / Q000378:metabolism; D051381:Rats; D019324:beta-Naphthoflavone
D001571:Benzoflavones; D007527:Isoenzymes; D009281:Naphthalenes; C029905:2,5-dichlorobiphenyl; D019324:beta-Naphthoflavone; D003577:Cytochrome P-450 Enzyme System; D011078:Polychlorinated Biphenyls; D004851:Epoxide Hydrolases; C030375:2,3-dichlorobiphenyl; D010634:Phenobarbital